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重组人亲环素A的表达、纯化及鉴定

[Expression, purification and characterization of recombinant human cyclophilin A].

作者信息

Li F, Zhao Q, Wu J, Shan X

机构信息

Center of Medical Laboratory Sciences of PLA, Jinling Hospital, Nanjing 210002.

出版信息

Wei Sheng Wu Xue Bao. 1998 Jun;38(3):193-6.

PMID:12549331
Abstract

Plasmid-derived expression of the human CyPA in E. coli would make it possible to obtain ample protein quantities and to avoid difficult task of obtaining human tissues for protein purification. The cDNA encoding human CyPA from MT4 lymph cell line has been cloned and an expression vector (pET11/CyPA) has been constructed under control of the T7 promoter for efficient expression in E. coli. The recombinant CyPA is produced at 41% of total soluble cell protein, and showed the peptidyl-prodyl cis-trans isomerase activity.

摘要

在大肠杆菌中通过质粒衍生表达人亲环素A(CyPA),将有可能获得大量蛋白质,并避免为蛋白质纯化而获取人体组织这一艰巨任务。已从MT4淋巴细胞系克隆了编码人CyPA的cDNA,并构建了一个在T7启动子控制下用于在大肠杆菌中高效表达的表达载体(pET11/CyPA)。重组CyPA的产量占总可溶性细胞蛋白的41%,并表现出肽基-脯氨酰顺反异构酶活性。

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